Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.

Abstract:

:Upon dimerization by oxidation, Hsp33 functions as a molecular chaperone in prokaryotes. Previously published structures of both the inactive and active species are of doubtful relevance to the solution conformations since the inactive (reduced) crystal structure was dimeric, while the active (oxidized) species was crystallized with a truncation of its regulation domain. The interdomain contact site of the inactive monomer, identified in this work, is consistent with that previously observed in the reduced dimer crystal. In contrast, fluorescence quenching of the active dimer contradicted the results expected from the domain-swapped fold observed in the truncated dimer crystal. The results of this study provide important new information concerning controversial issues in the activation process of Hsp33.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lee YS,Ryu KS,Kim SJ,Ko HS,Sim DW,Jeon YH,Kim EH,Choi WS,Won HS

doi

10.1016/j.febslet.2012.01.011

subject

Has Abstract

pub_date

2012-02-17 00:00:00

pages

411-5

issue

4

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00031-2

journal_volume

586

pub_type

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